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Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters

Nature Structural & Molecular Biology volume 20, pages 766–768 (2013)Cite this article

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Abstract

Here we present two structures of the major facilitator (MFS) xylose transporter XylE from Escherichia coli in inward open and partially occluded inward open conformations. These structures provide key information about the transport cycle of XylE and the closely related human GLUT transporters. This is, to our knowledge, the first MFS transporter structure determined in more than one conformational state, which may establish XylE as an important MFS model protein.

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Figure 1: Overview of conserved cytoplasmic motifs in selected members of the GLUT-homology family.
Figure 2: Overall structure of XylE.
Figure 3: Structural changes during the transport cycle.

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Acknowledgements

E.M.Q. was supported by The Danish Council for Independent Research (Medical Sciences; grant 271-09-0187). C.L. was supported by a European Molecular Biology Organization postdoctoral fellowship. This research was further supported by grants from the Swedish Research council, the Swedish Cancer Society and the integrated EU project European drug initiative on channels and transporters (EDICT), as well as a Singapore National Research Foundation Competitive Research Programme grant (NRF2008NRF-CRP002-067). We thank Diamond Light Source for access to beamline I02 (MX5873 and MX6603) that contributed to the results presented here and acknowledge the SOLEIL synchrotron for provision of synchrotron radiation facilities at beamline PROXIMA1 (proposal 20110314). We also thank the Protein Science Facility at the Karolinska Institute for provision of crystallization infrastructure.

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  1. Esben M Quistgaard and Christian Löw: These authors contributed equally to this work.

Authors and Affiliations

  1. Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden

    Esben M Quistgaard, Christian Löw, Per Moberg, Lionel Trésaugues & Pär Nordlund

  2. School of Biological Sciences, Nanyang Technological University, Singapore

    Pär Nordlund

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  1. Esben M Quistgaard
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  2. Christian Löw
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  3. Per Moberg
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Contributions

E.M.Q., C.L. and P.M. conducted experiments. L.T. assisted in data collection and analysis. E.M.Q. and C.L. wrote the initial manuscript, and L.T. and P.N. contributed with revisions. P.N. supervised the project. All authors contributed to experimental design and have read and approved the final manuscript.

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Correspondence to Pär Nordlund.

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The authors declare no competing financial interests.

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Supplementary Figures 1–5 and Supplementary Table 1 (PDF 2120 kb)

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Quistgaard, E., Löw, C., Moberg, P. et al. Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters. Nat Struct Mol Biol 20, 766–768 (2013). https://doi.org/10.1038/nsmb.2569

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